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Fungal infections, especially candidiasis and aspergillosis, claim an unacceptably high fatality rate. The energy ATP that is necessary for fungal cell growth and function is synthesized mainly through oxidative phosphorylation, with the key enzyme being F1Fo-ATP synthase. But it remains unknown how...
2021-10-08 | MTBLS3332 | MetaboLights
The F1Fo-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex's membrane-embedded motor section forms a proteinaceous channel at the interface between Atp9-ring and Atp6. To pr...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-11-03 | PXD006249 | Pride
The mitochondrial F1FO-ATP synthase produces the bulk of cellular ATP. The soluble F1 domain contains the catalytic head that is linked via the central stalk and the peripheral stalk to the membrane embedded rotor of the Fo domain. The assembly of the F1 domain and its linkage to the peripheral stal...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-01-11 | PXD033024 | Pride
Defects of mitochondrial functions lead in humans to vast array of usually multisystemic pathologies and several hundreds of diseases resulting from various defects of mitochondria biogenesis and maintenance, defects of respiratory chain complexes (OXPHOS) or defects of individual mitochondrial prot...
ORGANISM(S): Homo sapiens 
F1FO-ATP synthases play a central role in cellular metabolism, making the energy of the protonmotive force across a membrane available for a large number of energy-consuming processes. We determined the single-particle cryo-EM structure of active dimeric ATP synthase from mitochondria of Polytomella...
ORGANISM(S): Polytomella parva 
2019-05-01 | PXD013530 | Pride
The F1Fo-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex's membrane-embedded motor section forms a proteinaceous channel at the interface between Atp9 ring and Atp6. To pr...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-11-03 | PXD007146 | Pride
Purified mitochondrial ATP synthase has been shown to form Ca2+-activated, large conductance channel activity similar to that of mitochondrial megachannel (MMC) or mitochondrial permeability transition pore (mPTP) but the oligomeric state required for channel formation is being debated. We reconstit...
ORGANISM(S): Sus scrofa domesticus (domestic pig) 
2020-01-13 | PXD016255 | Pride
The F1Fo-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex's membrane-embedded motor section forms a proteinaceous channel at the interface between Atp9 ring and Atp6. To pr...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-11-03 | PXD007155 | Pride
Mitochondrial cristae are polymorphic invaginations of the inner membrane that are the fabric of cellular respiration. Both the Mitochondrial Contact Site and Cristae Organization System (MICOS) and the F1FO-ATP synthase are vital for sculpting cristae by opposing membrane bending forces. While MICO...
ORGANISM(S): Trypanosoma brucei brucei TREU927 
2021-06-15 | PXD025109 | Pride
Fungal infections, especially for candidiasis and aspergillosis, claim an unacceptably high fatality. However, the determining mechanism that promote fungal lethal infections are still elusive. The energy ATP necessary for fungal cell growth and function is synthesized mainly through oxidative phosp...
ORGANISM(S): Candida albicans (Yeast) 
2021-09-16 | PXD024729 | Pride
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